CDC37 Protein Overview: Sequence, Structure, Function and Protein Interaction

CDC37 Protein Overview

CDC37 reagents

In in vitro assays, Stepanova et al. (1996) showed that CDC37 associated most efficiently with CDK4, less with CDK6 (603368) and CDK7 (601955), but not with CDK2 or CDK3. They determined that CDC37, CDK4, and HSP90 form a high molecular weight complex. The interactions between CDK4 and CDC37 and those between CDK4 and D-type cyclins were found to be mutually exclusive. Loss of association of CDC37 and CDK4 by pharmacologic disruption of HSP90 function led to reduced stability of newly synthesized CDK4. Stepanova et al. (1996) concluded that CDC37 and HSP90 are important for CDK4 stability and play a positive role in cell cycle progression. Chen et al. (2002) identified CDC37 and HSP90 as 2 additional components of the I-kappa-B kinase (IKK) complex. This complex also contains 2 catalytic subunits, IKK-alpha (600664) and IKK-beta (603258), and a regulatory subunit, NEMO (300248). Vaughan et al. (2008) stated that CDC37 is phosphorylated on ser13, probably by casein kinase II (see 115440), and that absence of this phosphorylation severely compromises CDC37 function. They showed that ser13 was phosphorylated in vivo in uncomplexed CDC37, in CDC37 in a binary complex with CDK4, and in CDC37 in a ternary complex with CDK4 and HSP90. Ser13 in the CDC37-CDK4-HSP90 complex was resistant to nonspecific phosphatases, but it was efficiently dephosphorylated by protein phosphatase-5 (PP5, or PPP5C; 600658), which did not dephosphorylate uncomplexed CDC37. CDC37 and PP5 associated in HSP90 complexes in yeast and in human tumor cells, and PP5 regulated phosphorylation of ser13 of CDC37 in vivo, directly affecting activation of protein kinases by CDC37-HSP90. Vaughan et al. (2008) proposed that a cyclic regulatory mechanism reverses constitutive CDC37 phosphorylation when CDC37 is engaged in HSP90 complexes.

CDC37 protein family

Belongs to the CDC37 family.

CDC37 protein name

Recommended name
Hsp90 co-chaperone Cdc37
Aliases
CDC37 (cell division cycle 37, S. cerevisiae, homolog), CDC37 cell division cycle 37 homolog, Hsp90 co-chaperone Cdc37, P50CDC37
Alternative name
Hsp90 chaperone protein kinase-targeting subunit p50Cdc37 Hsp90 co-chaperone Cdc37, N-terminally processed

CDC37 Protein Sequence

Species Human CDC37 protein
Length 378
Mass (Da) 44468
Sequence Human CDC37 protein sequence
Species Mouse CDC37 protein
Length 379
Mass (Da) 44593
Sequence Mouse CDC37 protein sequence
Species Rat CDC37 protein
Length 379
Mass (Da) 44510
Sequence Rat CDC37 protein sequence

CDC37 Protein Molecular Weight & PI

Hsp90 co-chaperone Cdc37 (Hsp90 chaperone protein kinase-targeting subunit) (p50Cdc37) [Contains: Hsp90 co-chaperone Cdc37, N-terminally processed] Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 1-378 Hsp90 co-chaperone Cdc37.

Molecular weight (Da)

44468.3

Theoretical pI

5.17

CDC37 Protein Structure

C-terminal domain of Cdc37 cochaperone
Deposited
2015-08-02   Released:  2015-10-07
Deposition Author(s)
Keramisanou, D., Dudhat, A., Pare, M.
Organism(s)
Homo sapiens
Expression System
Escherichia coli
Experimental Data Snapshot
Method
SOLUTION NMR
2N5X From PDB

Human CDC37 protein Secondary structure

CDC37 Protein Interaction

Recombinant CDC37 Protein Feature

CDC37 Protein, Human, Recombinant (GST Tag)

High Purity
> 85 % as determined by SDS-PAGE
Low Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method

Recombinant CDC37 protein citations

Title
FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation
Year
2014
Author
Huang, W;Ye, M;Zhang, LR;Wu, QD;Zhang, M;Xu, JH;Zheng, W;
Journal
Mol. Cancer

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